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Literature summary for 2.4.99.18 extracted from

  • Schulz, B.L.; Aebi, M.
    Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency (2009), Mol. Cell. Proteomics, 8, 357-364.
    View publication on PubMed
Search for more literature for 2.4.99.18

Cloned(Commentary)

Cloned (Comment) Organism
plasmids with subunit genes introduced into mutants lacking both subunits Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information strains with deleted OST3 and OST6 loci are grown with plasmids introducing either one of the subunits Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall Saccharomyces cerevisiae glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616 ?
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616 Saccharomyces cerevisiae ?
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 ?

Synonyms

Synonyms Comment Organism
oligosaccharyltransferase
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 Saccharomyces cerevisiae
OST subunit Ost3p and Ost6p Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function subunits Ost3p and Ost6p are necessary for efficient glycosylation of distinct defined glycosylation sites Saccharomyces cerevisiae